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PDBsum entry 1ttf
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References listed in PDB file
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Key reference
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Title
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The three-Dimensional structure of the tenth type III module of fibronectin: an insight into rgd-Mediated interactions.
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Authors
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A.L.Main,
T.S.Harvey,
M.Baron,
J.Boyd,
I.D.Campbell.
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Ref.
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Cell, 1992,
71,
671-678.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of the tenth type III module of fibronectin has been
determined using nuclear magnetic resonance techniques. The molecule has a fold
similar to that of immunoglobulin domains, with seven beta strands forming two
antiparallel beta sheets, which pack against each other. Both beta sheets
contribute conserved hydrophobic residues to a compact core. The topology is
more similar to that of domain 2 of CD4, PapD, and the extracellular domain of
the human growth hormone receptor than to that of immunoglobulin C domains. The
module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion.
This tripeptide is solvent exposed and lies on a conformationally mobile loop
between strands F and G, consistent with its cell adhesion function.
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Figure 1.
Figure 1. The Structure of the Tenth Tpe ftl Module of Fibronectin
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Figure 5.
Figure 5. Folds of Similar Topology o the Type ll Module
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1992,
71,
671-678)
copyright 1992.
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Secondary reference #1
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Title
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1h nmr assignment and secondary structure of the cell adhesion type III module of fibronectin.
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Authors
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M.Baron,
A.L.Main,
P.C.Driscoll,
H.J.Mardon,
J.Boyd,
I.D.Campbell.
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Ref.
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Biochemistry, 1992,
31,
2068-2073.
[DOI no: ]
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PubMed id
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